Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.

Hydrogen deuterium exchange mass spectrometry (HDX-MS) is a powerful biophysical technique being increasingly applied to a wide variety of problems. As the HDX-MS community continues to grow, adoption of best practices in data collection, analysis, presentation and interpretation will greatly enhance the accessibility of this technique to nonspecialists. Here we provide recommendations arising from community discussions emerging out of the first International Conference on Hydrogen-Exchange Mass Spectrometry (IC-HDX; 2017). It is meant to represent both a consensus viewpoint and an opportunity to stimulate further additions and refinements as the field advances

How do proteins do all of that as seen by hydrogen exchange. Protein folding, GroEL function, lipoprotein structure

S. Walter Englander, Jacob Gershon-Cohen Professor of Medical Science, Professor of Biochemistry and Biophysics, University of Pennsylvania School of Medicine presented a lecture on May 10, 2011 from 11:00 AM to 12:00 PM in the Klaus Advanced Computing Building, Room 1116E.Runtime: 63:21 minutes.The talk will illustrate the use of hydrogen exchange methods to learn about biophysical properties and functional behaviors of protein molecules. Hydrogen exchange has been measured by older tritium exchange techniques, by 2D NMR, and most recently by mass spectrometry. Examples of applications will illustrate how each method provides specific advantages for different applications. Topics to be considered include how proteins fold, and how GroEL helps proteins to fold. Also recent progress in extending hydrogen exchange to the study of large and even insoluble protein systems using mass spectrometry will be shown